[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleActivation and closed-state inactivation mechanisms of the human voltage-gated K4 channel complexes.
Journal, issue, pagesMol Cell, Vol. 82, Issue 13, Page 2427-22442.e4, Year 2022
Publish dateJul 7, 2022
AuthorsWenlei Ye / Hongtu Zhao / Yaxin Dai / Yingdi Wang / Yu-Hua Lo / Lily Yeh Jan / Chia-Hsueh Lee /
PubMed AbstractThe voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion ...The voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion conduction and is as crucial to membrane excitability as activation. Inactivation can occur when the channel is open or closed. Although open-state inactivation is well understood, the molecular basis of closed-state inactivation has remained elusive. We report cryo-EM structures of human K4.2 channel complexes in inactivated, open, and closed states. Closed-state inactivation of K4 involves an unprecedented symmetry breakdown for pore closure by only two of the four S4-S5 linkers, distinct from known mechanisms of open-state inactivation. We further capture K4 in a putative resting state, revealing how voltage sensor movements control the pore. Moreover, our structures provide insights regarding channel modulation by KChIP2 and DPP6 auxiliary subunits. Our findings elucidate mechanisms of closed-state inactivation and voltage-dependent activation of the K4 channel.
External linksMol Cell / PubMed:35597238 / PubMed Central
MethodsEM (single particle)
Resolution2.24 - 3.02 Å
Structure data

26575

7uk5

EMDB-26575, PDB-7uk5:
Human Kv4.2-KChIP2 channel complex in an open state, transmembrane region
Method: EM (single particle) / Resolution: 2.76 Å

26576

7ukc

EMDB-26576, PDB-7ukc:
Human Kv4.2-KChIP2 channel complex in an inactivated state, class 1, transmembrane region
Method: EM (single particle) / Resolution: 3.0 Å

26577

7ukd

EMDB-26577, PDB-7ukd:
Human Kv4.2-KChIP2 channel complex in an inactivated state, class 2, transmembrane region
Method: EM (single particle) / Resolution: 2.88 Å

26578

7uke

EMDB-26578, PDB-7uke:
Human Kv4.2-KChIP2 channel complex in an intermediate state, transmembrane region
Method: EM (single particle) / Resolution: 3.01 Å

26579

7ukf

EMDB-26579, PDB-7ukf:
Human Kv4.2-KChIP2 channel complex in a putative resting state, transmembrane region
Method: EM (single particle) / Resolution: 3.02 Å

26580

7ukg

EMDB-26580, PDB-7ukg:
Human Kv4.2-KChIP2-DPP6 channel complex in an open state, transmembrane region
Method: EM (single particle) / Resolution: 2.24 Å

26581

7ukh

EMDB-26581, PDB-7ukh:
Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region
Method: EM (single particle) / Resolution: 2.33 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HG:
Unknown entry / Mercury (element)

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / potassium channel complex / MEMBRANE PROTEIN

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more